Heparin was modified at carboxyl groups by reaction with several pharmacologically important amino-containing compounds in aqueous medium in the presence of 1-ethyl-3-[3-(dimethylamino)propyl]carbodiimide. In dependence on the nature of the amine and the ratio of reagents, conjugates containing 36-100% amide and 0-25% isoureidocarbonyl groups were synthesized. Isoureidoarylamide groups are present, along with amide moieties, in the products of heparin modification by hydroxyl-containing aromatic amines. The conjugate of heparin with p-aminobenzoic acid contained oligomeric arylamide.

Download full-text PDF

Source

Publication Analysis

Top Keywords

[chemical modification
4
modification heparin]
4
heparin] heparin
4
heparin modified
4
modified carboxyl
4
carboxyl groups
4
groups reaction
4
reaction pharmacologically
4
pharmacologically amino-containing
4
amino-containing compounds
4

Similar Publications

Enhancing electrocatalytic hydrogen evolution engineering unsaturated electronic structures in MoS.

Chem Sci

December 2024

Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University Beijing 100871 China

The search for efficient, earth-abundant electrocatalysts for the hydrogen evolution reaction (HER) has identified unsaturated molybdenum disulfide (MoS) as a leading candidate. This review synthesises recent advancements in the engineering of MoS to enhance its electrocatalytic properties. It focuses on strategies for designing an unsaturated electronic structure on metal catalytic centers and their role in boosting the efficiency of the hydrogen evolution reaction (HER).

View Article and Find Full Text PDF

Bioorthogonal chemistry, recognized as a highly efficient tool in chemical biology, has shown significant value in cancer treatment. The primary objective is to develop efficient delivery strategies to achieve enhanced bioorthogonal drug treatment for tumors. Here, Janus microparticles (JMs) loaded with cyclooctene-modified doxorubicin prodrug (TCO-DOX) and tetrazine-modified indocyanine green (Tz-ICG) triggers are reported.

View Article and Find Full Text PDF

Factors influencing surimi gelling properties and natural additive-based gel fortification strategies: A review.

Compr Rev Food Sci Food Saf

January 2025

Aquatic Products Processing Factory of China National Zhoushan Marine Fisheries Company, Zhoushan, China.

Gelation and gel properties are crucial to surimi-based seafood products, and many factors significantly influence surimi gel quality. Although physical and chemical modifications can improve surimi gel performance, challenges such as high cost, difficulties in industrialization and environmental pollution pose significant barriers to their practicality. Natural additives offer a promising alternative by reinforcing and improving the characteristics of surimi gel through mechanisms such as protein conformational transformation, protein denaturation, and altered chemical forces.

View Article and Find Full Text PDF

Manipulating metal-ligand binding in allosteric coordination complexes through ring strain.

Chem Commun (Camb)

January 2025

Department of Chemistry and International Institute for Nanotechnology, Northwestern University, Evanston, Illinois 60208, USA.

The weak-link approach (WLA) to organometallic complexes offers a powerful method to create allosteric shape-shifting coordination complexes. However, chemically tuning the metal-ligand interactions entails challenging syntheses. This study explores the influence of ring strain on the lability of the platinum-sulfur interaction within WLA complexes, providing a simpler alternative to chemical modifications.

View Article and Find Full Text PDF

Multifaceted roles of UFMylation in health and disease.

Acta Pharmacol Sin

January 2025

Center for Cell Structure and Function, Shandong Provincial Key Laboratory of Animal Resistance Biology, College of Life Sciences, Shandong Normal University, Jinan, 250014, China.

Ubiquitin fold modifier 1 (UFM1) is a newly identified post-translational modifier that is involved in the UFMylation process. Similar to ubiquitination, UFMylation enables the conjugation of UFM1 to specific target proteins, thus altering their stability, activity, or localization. UFM1 chains have the potential to undergo cleavage from their associated proteins via UFM1-specific proteases, thus highlighting a reversible feature of UFMylation.

View Article and Find Full Text PDF

Want AI Summaries of new PubMed Abstracts delivered to your In-box?

Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!